Stabilization of the Escherichia coli elongation factor Tu-GTP-aminoacyl-tRNA complex
Author:
Publisher
Elsevier BV
Subject
Molecular Biology,Biochemistry,Biophysics
Reference25 articles.
1. Molecular Mechanism of Protein Biosynthesis;Miller,1977
2. Evidence for a guanine nucleotide-aminoacyl-RNA complex as an intermediate in the enzymatic transfer of aminoacyl-RNA to ribosomes
3. Aminoacyl-tRNA-Tu-GTP interaction with ribosomes
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1. Structural dynamics of translation elongation factor Tu during aa-tRNA delivery to the ribosome;Nucleic Acids Research;2018-08-11
2. A monovalent cation acts as structural and catalytic cofactor in translational GTP ases;The EMBO Journal;2014-09-15
3. Recognition of Aminoacyl-tRNAs by Protein Elongation Factors;tRNA;2014-04-30
4. e IF 5 B employs a novel domain release mechanism to catalyze ribosomal subunit joining;The EMBO Journal;2014-04
5. Elongation Factor Ts Directly Facilitates the Formation and Disassembly of the Escherichia coli Elongation Factor Tu·GTP·Aminoacyl-tRNA Ternary Complex;Journal of Biological Chemistry;2013-05
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